Several cell surface associated proteins of the Staphylococci and Streptococci involved in microbial adhesion to different host tissues and considered to be important factors in bacterial pathogenesis have been identified in the last decade (see Patti, J. M., Allen, B. L., McGavin, M. J. and Hook, M., MSCRAMM-Mediated Adherence of Microorganisms to Host Tissues 1994! Annu. Rev. Microbiol. 48,585-617.).
The cell surface proteins fibronectin binding protein, fibrinogen binding protein, collagen binding protein and protein A of Staphylococcus aureus have all been identified as having peptidoglycan spanning regions rich in proline and glycine residues, N-terminal to the LPXTG motif characteristic of surface proteins in gram-positive bacteria (see Surface-associated proteins of Staphylococcus aureus: Their possible roles in virulence. Foster,T. J. and McDevitt, D. 1994! FEMS Microbiology Letters 118, 199-206).
Different approaches have been put forward to address such proteins from Staphylococcus aureus as antibacterial targets, e.g. fibronectin binding proteins (EP0294349, EP0397633, WO94/18327), fibrinogen binding protein (WO94/06830), collagen binding protein (WO92/07002) and bone sialoprotein binding protein (WO94/13310). The binding proteins or binding fragments thereof are used as antibacterial agents to block binding of the organism to host tissue, as vaccines to raise antibodies to the organism in the host animal or as antigens to raise therapeutic antibodies which can be used to block binding of the organism to host tissue.